[1]	NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEIN SEQUENCE OF 34-67; 92-118 AND 146-158, IDENTIFICATION IN A COMPLEX WITH FGF1 AND FGF2, INTERACTION WITH FGF1, AND TISSUE SPECIFICITY. TISSUE=Epidermal carcinoma; PubMed=1885605 [NCBI, ExPASy, EBI, Israel, Japan] Wu D.Q., Kan M.K., Sato G.H., Okamoto T., Sato J.D.; "Characterization and molecular cloning of a putative binding protein for heparin-binding growth factors."; J. Biol. Chem. 266:16778-16785(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Shi S., Sato J.D.; "Gene sequence for the human FGF-binding protein HBp17."; Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Ovary, and Pancreas; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[4]	FUNCTION. DOI=10.1038/nm1097-1137; PubMed=9334727 [NCBI, ExPASy, EBI, Israel, Japan] Czubayko F., Liaudet-Coopman E.D., Aigner A., Tuveson A.T., Berchem G.J., Wellstein A.; "A secreted FGF-binding protein can serve as the angiogenic switch in human cancer."; Nat. Med. 3:1137-1140(1997).
[5]	INTERACTION WITH HSPG2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1074/jbc.M011493200; PubMed=11148217 [NCBI, ExPASy, EBI, Israel, Japan] Mongiat M., Otto J., Oldershaw R., Ferrer F., Sato J.D., Iozzo R.V.; "Fibroblast growth factor-binding protein is a novel partner for perlecan protein core."; J. Biol. Chem. 276:10263-10271(2001).
[6]	FUNCTION, AND INTERACTION WITH FGF2. DOI=10.1074/jbc.M104933200; PubMed=11509569 [NCBI, ExPASy, EBI, Israel, Japan] Tassi E., Al-Attar A., Aigner A., Swift M.R., McDonnell K., Karavanov A., Wellstein A.; "Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein."; J. Biol. Chem. 276:40247-40253(2001).
[7]	FUNCTION, INTERACTION WITH FGF7; FGF10 AND FGF22, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1038/sj.onc.1208560; PubMed=15806171 [NCBI, ExPASy, EBI, Israel, Japan] Beer H.-D., Bittner M., Niklaus G., Munding C., Max N., Goppelt A., Werner S.; "The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair."; Oncogene 24:5269-5277(2005).
[8]	INTERACTION WITH FGF2, AND MUTAGENESIS OF CYS-214. DOI=10.1074/jbc.M510754200; PubMed=16257968 [NCBI, ExPASy, EBI, Israel, Japan] Xie B., Tassi E., Swift M.R., McDonnell K., Bowden E.T., Wang S., Ueda Y., Tomita Y., Riegel A.T., Wellstein A.; "Identification of the fibroblast growth factor (FGF)-interacting domain in a secreted FGF-binding protein by phage display."; J. Biol. Chem. 281:1137-1144(2006).

Comments

FUNCTION: Acts as a carrier protein that release fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhance the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth.
SUBUNIT: Found in a complex with FGFBP1, FGF1 and FGF2. Interacts with FGF1, FGF2, FGF7, FGF10, FGF22 and HSPG2.
INTERACTION:
P09038:FGF2; NbExp=3; IntAct=EBI-953742, EBI-977447;
SUBCELLULAR LOCATION: Secreted, extracellular space. Cell membrane; Peripheral membrane protein. Note=Extracellular and plasma membrane-associated. Colocalizes with HSPG2 in the pericellular environment of squamous cell carcinomas.
TISSUE SPECIFICITY: Expressed in the suprabasal region of the epidermis, in hair follicles, the basement membrane at the dermo-epidermal junction (occasionally extending into the basement membrane of dermal blood vessels), wounded skin and several invasive squamous cell carcinomas (at protein level). Expressed in normal and wounded skin and various squamous cell carcinomas.
INDUCTION: Up-regulated in epithelial cells after skin injury. Keratinocyte mitogens.
MISCELLANEOUS: Expression is significantly up-regulated in carcinogen-induced skin tumors, various squamous cell carcinomas, some colon cancer cell lines and tumors.
SIMILARITY: Belongs to the fibroblast growth factor-binding protein family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M60047; AAA58636.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF149412; AAD39216.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003628; AAH03628.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008910; AAH08910.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A41178; A41178.

NP_005121.1; -.

3D structure databases

ModBase

Q14512.

Protein-protein interaction databases

IntAct

Q14512; -.

PTM databases

PhosphoSite

Q14512; -.

Organism-specific databases

HIX0004114; -.

HGNC:19695; FGFBP1.

HPA004332; -.

607737; gene. [NCBI / EBI]

PharmGKB

PA134880558; -.

GeneCards

Q14512.

Gene expression databases

ArrayExpress

Q14512; -.

CleanEx

HS_FGFBP1; -.

GermOnline

ENSG00000137440; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0008201;	Molecular function: heparin binding (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007267;	Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0008285;	Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0007165;	Biological process: signal transduction (non-traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR010510; FGF1_bd.
Graphical view of domain structure.

PANTHER

PTHR15258; FGF1_bd; 1.

Pfam

PF06473; FGF-BP1; 1.
Pfam graphical view of domain structure.

BLOCKS

Q14512.

Genome annotation databases

Ensembl

ENSG00000137440; Homo sapiens. [Contig view]

GeneID

9982; -.

KEGG

hsa:9982; -.

Phylogenomic databases

HOGENOM

Q14512; -.

HOVERGEN

Q14512; -.

Other

SOURCE

FGFBP1; Homo sapiens.

ProtoNet

Q14512.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cell membrane; Direct protein sequencing; Glycoprotein; Growth factor binding; Membrane; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 234`	`211`	`Fibroblast growth factor-binding protein 1.`	`PRO_0000245512`
`REGION`	`193 234`	`42`	`Sufficient for interaction with FGF2 and FGF2-induced effects.`
`CARBOHYD`	`169 169`		`O-linked (GalNAc...) (By similarity).`
`DISULFID`	`68 85`		`By similarity.`
`DISULFID`	`94 127`		`By similarity.`
`DISULFID`	`103 139`		`By similarity.`
`DISULFID`	`197 234`		`By similarity.`
`DISULFID`	`214 222`		`By similarity.`
`MUTAGEN`	`214 214`		`C->A: Strongly reduces interaction with FGF2.`

Sequence information

Length: 234 AA [This is the length of the unprocessed precursor]

Molecular weight: 26264 Da [This is the MW of the unprocessed precursor]

CRC64: AAF4209F29F2D058 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKICSLTLLS FLLLAAQVLL VEGKKKVKNG LHSKVVSEQK DTLGNTQIKQ KSRPGNKGKF 

        70         80         90        100        110        120 
VTKDQANCRW AATEQEEGIS LKVECTQLDH EFSCVFAGNP TSCLKLKDER VYWKQVARNL 

       130        140        150        160        170        180 
RSQKDICRYS KTAVKTRVCR KDFPESSLKL VSSTLFGNTK PRKEKTEMSP REHIKGKETT 

       190        200        210        220        230 
PSSLAVTQTM ATKAPECVED PDMANQRKTA LEFCGETWSS LCTFFLSIVQ DTSC

Q14512 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools